3TMK
CRYSTAL STRUCTURE OF YEAST THYMIDYLATE KINASE COMPLEXED WITH THE BISUBSTRATE INHIBITOR TP5A AT 2.0 A RESOLUTION: IMPLICATIONS FOR CATALYSIS AND AZT ACTIVATION
Summary for 3TMK
Entry DOI | 10.2210/pdb3tmk/pdb |
Descriptor | THYMIDYLATE KINASE, P1-(5'-ADENOSYL)P5-(5'-THYMIDYL)PENTAPHOSPHATE (3 entities in total) |
Functional Keywords | kinase, phosphotransferase |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Total number of polymer chains | 8 |
Total formula weight | 204885.83 |
Authors | Lavie, A.,Schlichting, I.,Konrad, M.,Goody, R.S.,Brundiers, R.,Reinstein, J. (deposition date: 1998-01-26, release date: 1999-02-16, Last modification date: 2024-05-22) |
Primary citation | Lavie, A.,Konrad, M.,Brundiers, R.,Goody, R.S.,Schlichting, I.,Reinstein, J. Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-thymidyl) pentaphosphate (TP5A) at 2.0 A resolution: implications for catalysis and AZT activation. Biochemistry, 37:3677-3686, 1998 Cited by PubMed: 9521686DOI: 10.1021/bi9720787 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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